CA2402066A1 - Proteines pharmaceutiques, agents therapeutiques humains, albumine serique humaine, insuline, et toxique b de cholera natif soumis a des plastes transgeniques - Google Patents

Proteines pharmaceutiques, agents therapeutiques humains, albumine serique humaine, insuline, et toxique b de cholera natif soumis a des plastes transgeniques Download PDF

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Publication number: CA2402066A1
Authority: CA; Canada
Prior art keywords: plastid; sequence; flanking; expression; protein
Prior art date: 2000-03-01
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Granted

Application number

CA002402066A

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English (en)

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CA2402066C (fr

Inventor

Henry Daniell

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Auburn University

University of Pennsylvania Penn

Original Assignee

Individual

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

2000-03-01

Filing date

2001-02-28

Publication date

2001-10-04

2001-02-28 Application filed by Individual filed Critical Individual

2001-10-04 Publication of CA2402066A1 publication Critical patent/CA2402066A1/fr

2015-09-29 Application granted granted Critical

2015-09-29 Publication of CA2402066C publication Critical patent/CA2402066C/fr

2021-02-28 Anticipated expiration legal-status Critical

Status Expired - Lifetime legal-status Critical Current

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- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
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- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/28—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Vibrionaceae (F)
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- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/62—Insulins
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/76—Albumins
- C07K14/765—Serum albumin, e.g. HSA
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- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
- C12N15/8201—Methods for introducing genetic material into plant cells, e.g. DNA, RNA, stable or transient incorporation, tissue culture methods adapted for transformation
- C12N15/8214—Plastid transformation
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- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
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- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
- C12N15/8241—Phenotypically and genetically modified plants via recombinant DNA technology
- C12N15/8242—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits
- C12N15/8257—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits for the production of primary gene products, e.g. pharmaceutical products, interferon
- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/20—Fusion polypeptide containing a tag with affinity for a non-protein ligand
- C07K2319/21—Fusion polypeptide containing a tag with affinity for a non-protein ligand containing a His-tag
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/35—Fusion polypeptide containing a fusion for enhanced stability/folding during expression, e.g. fusions with chaperones or thioredoxin
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/50—Fusion polypeptide containing protease site
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/55—Fusion polypeptide containing a fusion with a toxin, e.g. diphteria toxin
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
- C07K2319/75—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor containing a fusion for activation of a cell surface receptor, e.g. thrombopoeitin, NPY and other peptide hormones

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Microbiology (AREA)
Physics & Mathematics (AREA)
Plant Pathology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Gastroenterology & Hepatology (AREA)
Toxicology (AREA)
Cell Biology (AREA)
Pharmacology & Pharmacy (AREA)
Endocrinology (AREA)
Diabetes (AREA)
Peptides Or Proteins (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Breeding Of Plants And Reproduction By Means Of Culturing (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)

CA2402066A 2000-03-01 2001-02-28 Proteines pharmaceutiques, agents therapeutiques humains, albumine serique humaine, insuline, et toxique b de cholera natif soumis a des plastes transgeniques Expired - Lifetime CA2402066C (fr)

Applications Claiming Priority (11)

Application Number	Priority Date	Filing Date	Title
US18598700P	2000-03-01	2000-03-01
US60/185,987		2000-03-01
US26342401P	2001-01-23	2001-01-23
US26347301P	2001-01-23	2001-01-23
US26366801P	2001-01-23	2001-01-23
US60/263,473		2001-01-23
US60/263,668		2001-01-23
US60/263,424		2001-01-23
US27068101P	2001-02-22	2001-02-22
US60/270,681		2001-02-22
PCT/US2001/006288 WO2001072959A2 (fr)	2000-03-01	2001-02-28	Proteines pharmaceutiques, agents therapeutiques humains, albumine serique humaine, insuline, et toxique b de cholera natif soumis a des plastes transgeniques

Publications (2)

Publication Number	Publication Date
CA2402066A1 true CA2402066A1 (fr)	2001-10-04
CA2402066C CA2402066C (fr)	2015-09-29

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Application Number	Title	Priority Date	Filing Date
CA2402066A Expired - Lifetime CA2402066C (fr)	2000-03-01	2001-02-28	Proteines pharmaceutiques, agents therapeutiques humains, albumine serique humaine, insuline, et toxique b de cholera natif soumis a des plastes transgeniques

Country Status (6)

Country	Link
US (1)	US20100304476A1 (fr)
EP (2)	EP2080803B1 (fr)
AT (1)	ATE510916T1 (fr)
AU (1)	AU2001276813A1 (fr)
CA (1)	CA2402066C (fr)
WO (1)	WO2001072959A2 (fr)

Families Citing this family (31)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US20100251425A9 (en)	1998-05-15	2010-09-30	University Of Central Florida	Expression of human interferon in transgenic chloroplasts
CA2437868A1 (fr) *	2001-02-14	2002-08-22	Ventria Bioscience	Expression de proteines de lait humain dans des plantes transgeniques
US7354760B2 (en)	2001-12-26	2008-04-08	University Of Central Florida Research Foundation, Inc.	Expression of protective antigens in transgenic chloroplasts
CA2471737C (fr)	2001-12-26	2016-01-26	University Of Central Florida	Expression d'antigenes protecteurs dans des chloroplastes transgeniques et production de vaccins ameliores
WO2003091413A2 (fr) *	2002-04-23	2003-11-06	The Scripps Research Institute	Expression de polypeptides dans des chloroplastes, et compositions et procedes permettant de les exprimer
AU2008202053B2 (en) *	2002-04-23	2012-11-01	The Scripps Research Institute	Expression of polypeptides in chloroplasts, and compositions and methods for expressing same
EP2308985B1 (fr)	2002-07-03	2018-06-06	The Trustees of the University of Pennsylvania	Production de plastes par genie genetique par l'intermediaire d'une embryogenese somatique
CA2491639A1 (fr)	2002-07-03	2004-01-15	University Of Central Florida	Expression de igf-1 humain dans des plastes transgeniques
CA2741545A1 (fr)	2003-03-28	2004-10-14	National Institute Of Agrobiological Sciences	Procede de production d'un organe de stockage vegetal avec une production elevee de proteines de recombinaison et nouvelle proteine de recombinaison
EA014887B1 (ru) *	2003-06-17	2011-02-28	Сембайосиз Джинетикс Инк.	Способ экспрессии инсулина в семенах растения, способ получения семян растений, содержащих инсулин, и растения, способные производить семена, содержащие инсулин
AU2003253807A1 (en) *	2003-07-03	2005-02-15	University Of Central Florida	A chloroplast transgenic approach to express and purify human serum albumin, a protein highly susceptible to proteolytic degradation
CA2608671C (fr)	2005-05-27	2018-05-15	University Of Central Florida	Chloroplastes genetiquement modifies pour exprimer des proteines pharmaceutiques
US20100015713A1 (en) *	2005-06-28	2010-01-21	Scott Deeter	Components of cell culture media produced from plant cells
CN1884517B (zh) *	2006-06-08	2010-06-30	武汉禾元生物科技有限公司	利用谷物非储藏蛋白为融合载体在胚乳表达多肽的方法及应用
US20090328249A1 (en) *	2006-07-07	2009-12-31	Eric Paget	Transplastomic Plants Expressing Lumen-Targeted Protein
AU2008232543B2 (en) *	2007-03-30	2013-01-17	University Of Central Florida Research Foundation, Inc.	Chloroplasts engineered to express pharmaceutical proteins in edible plants
CN101835901B (zh)	2007-06-01	2013-03-06	蓝宝石能源公司	遗传修饰的光合生物的高通量筛选
EP2203542A1 (fr)	2007-09-11	2010-07-07	Sapphire Energy, Inc.	Procédés de fabrication de produits organiques avec des organismes photosynthétiques, produits obtenus et compositions pour l'obtention de ceux-ci
JP2011511090A (ja)	2008-02-07	2011-04-07	セレジーンインコーポレイテッド	治療用タンパク質をコードする発現ベクターの硝子体内投与による光受容体のレスキュー方法
US10689633B2 (en)	2008-02-29	2020-06-23	The Trustees Of The University Of Pennsylvania	Expression of β-mannanase in chloroplasts and its utilization in lignocellulosic woody biomass hydrolysis
US20110110981A1 (en) *	2008-05-27	2011-05-12	Henry Daniell	Orally Administerable Vaccine for Yersinia Pestis
CH699512A2 (de) *	2008-09-05	2010-03-15	Plantcare Ag	Verfahren und Vorrichtung zur automatischen Regelung der Bewässerung von Pflanzen.
CN102369276B (zh)	2009-02-20	2015-02-04	文特里亚生物科学公司	含有蛋白质组合的细胞培养基
WO2011057243A2 (fr)	2009-11-09	2011-05-12	University Of Central Florida Research Foundation, Inc.	Administration par voie orale d'agents de tolérance exprimés chez les plantes
US10865419B2 (en)	2011-10-24	2020-12-15	The Trustees Of The University Of Pennsylvania	Orally administered plastid expressed cholera toxin B subunit-exendin 4 as treatment for type 2 diabetes
CN105452470A (zh)	2013-06-14	2016-03-30	杰.尔.辛普洛公司	在植物中生产蛋白质
WO2015058214A1 (fr)	2013-10-18	2015-04-23	Trustees Of The University Of Pennsylvania	Administration orale d'enzyme de conversion de l'angiotensine 2 (ace2) ou d'angiotensine-(1-7) bioencapsulée dans des cellules végétales
EP3068869B1 (fr)	2013-11-15	2020-07-22	The Trustees Of The University Of Pennsylvania	Compositions pour la suppression de la formation d'un inhibiteur contre le facteur viii de l'hémophilie a chez des patients par administration d'antigènes bioencapsulés dans des cellules végétales
JP2019503341A (ja)	2015-11-16	2019-02-07	ザトラスティーズオブザユニバーシティオブペンシルバニア	植物細胞に生物学的に封入された、治療用タンパク質の、疾患の治療のための関心のある細胞型への標的化された送達
WO2023130185A1 (fr) *	2022-01-07	2023-07-13	Solar Grants Biotechnology Inc.	Procédé de transformation génétique de génome d'organite végétal et ses utilisations
TW202417621A (zh) *	2022-10-18	2024-05-01	博唯弘展生技股份有限公司	在植物系統中生產重組人類凝血酶蛋白質及其應用

Family Cites Families (17)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4616078A (en) *	1985-04-08	1986-10-07	Eli Lilly And Company	Process for purifying proinsulin-like materials
US4956282A (en) *	1985-07-29	1990-09-11	Calgene, Inc.	Mammalian peptide expression in plant cells
US4963665A (en) *	1986-01-07	1990-10-16	Washington University	Human preproinsulin-like growth factor I
US6680426B2 (en)	1991-01-07	2004-01-20	Auburn University	Genetic engineering of plant chloroplasts
US5932479A (en) *	1988-09-26	1999-08-03	Auburn University	Genetic engineering of plant chloroplasts
US5693507A (en) *	1988-09-26	1997-12-02	Auburn University	Genetic engineering of plant chloroplasts
US5877402A (en) *	1990-05-01	1999-03-02	Rutgers, The State University Of New Jersey	DNA constructs and methods for stably transforming plastids of multicellular plants and expressing recombinant proteins therein
US6004782A (en) *	1995-04-14	1999-12-21	Bioelastics Research Ltd.	Hyperexpression of bioelastic polypeptides
EP1002115B9 (fr) *	1997-08-07	2008-12-03	Auburn University	Vecteurs universels d'integration et d'expression de chloroplastes et plantes transformees
AU1072499A (en) *	1997-10-07	1999-04-27	Loma Linda University	Expression of cholera toxin b subunit in transgenic plants and efficacy thereof in oral vaccines
BR9912019A (pt) *	1998-07-10	2002-02-19	Calgene Llc	Expressão de peptìdeos de eucarióticos em plastìdeos de plantas
US6541682B1 (en) *	1998-11-12	2003-04-01	Calgene Llc	Plastid transformation of solanaceous plants
AU2001245358A1 (en) *	2000-02-29	2001-09-12	Auburn University	Production of antibodies in transgenic plastids
EP1294221A4 (fr)	2000-03-02	2003-06-25	Univ Auburn	Plantes transgeniques sans marqueurs: manipulation du genome chloroplastique sans selection antibiotique
CA2471737C (fr)	2001-12-26	2016-01-26	University Of Central Florida	Expression d'antigenes protecteurs dans des chloroplastes transgeniques et production de vaccins ameliores
US7767885B2 (en)	2001-12-26	2010-08-03	University Of Central Florida Research Foundation, Inc.	Plastid genetic engineering via somatic embryogenesis
AU2003253781A1 (en)	2002-07-03	2004-01-23	University Of Central Florida	Expression of human interferon in transgenic chloroplasts

2001
- 2001-02-28 EP EP08020922A patent/EP2080803B1/fr not_active Expired - Lifetime
- 2001-02-28 EP EP01954572A patent/EP1274846A4/fr not_active Ceased
- 2001-02-28 AU AU2001276813A patent/AU2001276813A1/en not_active Abandoned
- 2001-02-28 CA CA2402066A patent/CA2402066C/fr not_active Expired - Lifetime
- 2001-02-28 AT AT08020922T patent/ATE510916T1/de not_active IP Right Cessation
- 2001-02-28 WO PCT/US2001/006288 patent/WO2001072959A2/fr not_active Ceased
2010
- 2010-05-18 US US12/781,944 patent/US20100304476A1/en not_active Abandoned

Also Published As

Publication number	Publication date
EP1274846A4 (fr)	2004-09-29
CA2402066C (fr)	2015-09-29
US20100304476A1 (en)	2010-12-02
EP1274846A2 (fr)	2003-01-15
WO2001072959A2 (fr)	2001-10-04
WO2001072959A3 (fr)	2002-05-10
EP2080803B1 (fr)	2011-05-25
EP2080803A1 (fr)	2009-07-22
AU2001276813A1 (en)	2001-10-08
ATE510916T1 (de)	2011-06-15

Publication	Publication Date	Title
CA2402066C (fr)	2015-09-29	Proteines pharmaceutiques, agents therapeutiques humains, albumine serique humaine, insuline, et toxique b de cholera natif soumis a des plastes transgeniques
US20060117412A1 (en)	2006-06-01	Pharmaceutical proteins, human therapeutics, human serum albumin insulin, native cholera toxic B submitted on transgenic plastids
US20190390217A1 (en)	2019-12-26	Pharmaceutical proteins, human therapeutics, human serum albumin insulin, native cholera toxin b subunit on transgenic plastids
Arakawa et al.	1997	Expression of cholera toxin B subunit oligomers in transgenic potato plants
Daniell et al.	2001	Expression of the native cholera toxin B subunit gene and assembly as functional oligomers in transgenic tobacco chloroplasts
Makhzoum et al.	2014	Recent advances on host plants and expression cassettes' structure and function in plant molecular pharming
Patel et al.	2007	Elastin-like polypeptide fusions enhance the accumulation of recombinant proteins in tobacco leaves
Chebolu et al.	2009	Chloroplast-derived vaccine antigens and biopharmaceuticals: expression, folding, assembly and functionality
Daniell et al.	2004	Chloroplast derived antibodies, biopharmaceuticals and edible vaccines
Li et al.	2006	Expression of cholera toxin B subunit and the B chain of human insulin as a fusion protein in transgenic tobacco plants
Arakawa et al.	1999	Food plant-delivered cholera toxin B subunit for vaccination and immunotolerization
AU2009200434B2 (en)	2012-03-22	Process for producing plant storage organ with high production of recombinant protein and novel recombinant protein
US7741536B2 (en)	2010-06-22	Expression of human serum albumin in plastids
Kang et al.	2004	Modification of the cholera toxin B subunit coding sequence to enhance expression in plants
CA2608671A1 (fr)	2007-05-10	Chloroplastes genetiquement modifies pour exprimer des proteines pharmaceutiques
NZ547006A (en)	2009-03-31	Chimeric carrier molecules for the production of mucosal vaccines
WO1999018225A1 (fr)	1999-04-15	Expression de la sous-unite de la toxine b du cholera chez les plantes transgeniques et son efficacite dans les vaccins oraux
AU2007200503B2 (en)	2010-01-28	Pharmaceutical proteins, human therapeutics, human serum albumin insulin, native cholera toxin B subunit on transgenic plastids
US7554006B2 (en)	2009-06-30	Commercial production of insulin and insulin-like protein in plants
Gao et al.	2012	[Retracted] Stable Plastid Transformation for High‐Level Recombinant Protein Expression: Promises and Challenges
WO2001016339A1 (fr)	2001-03-08	Utilisation de constructions de fusion d'arabinogalactane dans un procede d'expression de proteines et de peptides dans des plantes
Zhao et al.	2009	Generation of transgenic cucumbers with expression of a ten-tandem repeat long-acting GLP-1 analogue and their biological function on diabetic rats
Devine	2006	Expression Of Heterologous Proteins In Transgenic Tobacco Chloroplasts To Produce A Biopharmaceutical And Biopolymer
Koya	2004	Evaluation of immunogenecity of transgenic chloroplast derived protective antigen of Bacillus anthracis
Koya	2004	Evaluation Of Immunogenicity Of Transgenic Chloroplast Derived Protect

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